Linked Life Data

20447866

Source:http://linkedlifedata.com/resource/pubmed/id/20447866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-8-3
pubmed:abstractText
The class IIa histone deacetylases (HDACs), HDAC4, 5, 7, and 9, have crucial roles in the development of the immune system and other organs, including brain, heart, and muscle. In addition to their catalytic domain, they are characterized by a large amino-terminal extension. The amino-terminal domain is subject to reversible phosphorylation, which controls their nucleo-cytoplasmic distribution. Unphosphorylated, class IIa HDACs remain in the nucleus, bound to chromatin, and repress transcription. Upon phosphorylation, they shuttle out of the nucleus, allowing derepression of their target genes. Thus, the nucleo-cytoplasmic translocation is associated with derepression of target genes. Recent studies identified the kinases and phosphatases that regulate the nucleo-cytoplasmic shuttling of class IIa HDACs. Here we will summarize this rapidly evolving field with a particular focus on the immune system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1471-4973
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
454-60
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Regulatory signal transduction pathways for class IIa histone deacetylases.
pubmed:affiliation
Cellular Differentiation Group, Cancer Epigenetics and Biology Program (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), Av. Gran Via s/n km 2.7, 08907 L'Hospitalet, Barcelona, Spain.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't